P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG

Autores
Fusco, Luciano Sebastian; Rodríguez, Juan Pablo; Torres Huaco, Frank; Huancahuire Vega, Salomón; Teibler, Gladys Pamela; Acosta, Ofelia Cristina; Marangoni, Sergio; Ponce Soto, Luis; Leiva, Laura Cristina Ana
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Four proteins with phospholipase A2 (PLA2) activity, designated P9a(Cdt-PLA2), P9b(Cdt-PLA2), P10a(Cdt-PLA2) and P10b(Cdt-PLA2) were purified from the venom of Crotalus durissus terrificus by two chromatographic steps: a gel filtration and reversed phase HPLC. The profile obtained clearly shows that three of them have a similar abundance. The molecular mass, 14193.8340Da for P9a(Cdt-PLA2), 14134.9102Da for P9b(Cdt-PLA2), 14242.6289Da for P10a(Cdt-PLA2) and 14183.8730Da for P10b(Cdt-PLA2), were initially evaluated by SDS-PAGE and confirmed by ESI-Q-TOF spectrometry, and all of them displayed a monomeric conformation. Also, partial amino acid sequence of each protein was obtained and their alignments with other crotalic PLA2 revealed a high degree of identity among them. Additionally, we studied some pharmacological activities like neurotoxicity, myotoxicity and lethality, which prompted us to pick two of them, P9a(Cdt-PLA2) and P10a(Cdt-PLA2) that resulted to be less toxic that the others, and further characterize them to be used as immunogen. We next injected these last proteins in mice to produce antitoxins against them and ELISA and dot blots reveled that both toxins do not show immunogenic differences, unlike those other pharmacologic activities tested. Furthermore, the antibodies produced cross-reacted with all the isoforms purified demonstrating the feasibility of using only one of them and ensuring the cross-reaction of all.The results obtained show that P9a(Cdt-PLA2) isoform has the lowest toxicity and also a good purification performance; thus this protein may be a promising candidate to be employed in the production of crotalic antitoxins.
Fil: Fusco, Luciano Sebastian. Universidad Nacional del Nordeste. Facultad de Cs.exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación En Proteinas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Rodríguez, Juan Pablo. Universidad Nacional del Nordeste. Facultad de Cs.exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación En Proteinas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Torres Huaco, Frank. Universidade Estadual Do Campinas. Instituto de Biología; Brasil
Fil: Huancahuire Vega, Salomón. Universidade Estadual Do Campinas. Instituto de Biología; Brasil
Fil: Teibler, Gladys Pamela. Universidad Nacional del Nordeste. Facultad de Cs.veterinarias. Departamento de Clinica. Cátedra de Farmacología; Argentina
Fil: Acosta, Ofelia Cristina. Universidad Nacional del Nordeste. Facultad de Cs.veterinarias. Departamento de Clinica. Cátedra de Farmacología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marangoni, Sergio. Universidade Estadual Do Campinas. Instituto de Biología; Brasil
Fil: Ponce Soto, Luis. Universidade Estadual Do Campinas. Instituto de Biología; Brasil
Fil: Leiva, Laura Cristina Ana. Universidad Nacional del Nordeste. Facultad de Cs.exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación En Proteinas; Argentina
Materia
Antivenom
Hplc-Pr
Myotoxin
Neurotoxicity
Rattlesnake
Snake Venom
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/37476
Acceder
id CONICETDig_9156dfcc3228c11b44ad6093df4db80c
oai_identifier_str oai:ri.conicet.gov.ar:11336/37476
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgGFusco, Luciano SebastianRodríguez, Juan PabloTorres Huaco, FrankHuancahuire Vega, SalomónTeibler, Gladys PamelaAcosta, Ofelia CristinaMarangoni, SergioPonce Soto, LuisLeiva, Laura Cristina AnaAntivenomHplc-PrMyotoxinNeurotoxicityRattlesnakeSnake Venomhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Four proteins with phospholipase A2 (PLA2) activity, designated P9a(Cdt-PLA2), P9b(Cdt-PLA2), P10a(Cdt-PLA2) and P10b(Cdt-PLA2) were purified from the venom of Crotalus durissus terrificus by two chromatographic steps: a gel filtration and reversed phase HPLC. The profile obtained clearly shows that three of them have a similar abundance. The molecular mass, 14193.8340Da for P9a(Cdt-PLA2), 14134.9102Da for P9b(Cdt-PLA2), 14242.6289Da for P10a(Cdt-PLA2) and 14183.8730Da for P10b(Cdt-PLA2), were initially evaluated by SDS-PAGE and confirmed by ESI-Q-TOF spectrometry, and all of them displayed a monomeric conformation. Also, partial amino acid sequence of each protein was obtained and their alignments with other crotalic PLA2 revealed a high degree of identity among them. Additionally, we studied some pharmacological activities like neurotoxicity, myotoxicity and lethality, which prompted us to pick two of them, P9a(Cdt-PLA2) and P10a(Cdt-PLA2) that resulted to be less toxic that the others, and further characterize them to be used as immunogen. We next injected these last proteins in mice to produce antitoxins against them and ELISA and dot blots reveled that both toxins do not show immunogenic differences, unlike those other pharmacologic activities tested. Furthermore, the antibodies produced cross-reacted with all the isoforms purified demonstrating the feasibility of using only one of them and ensuring the cross-reaction of all.The results obtained show that P9a(Cdt-PLA2) isoform has the lowest toxicity and also a good purification performance; thus this protein may be a promising candidate to be employed in the production of crotalic antitoxins.Fil: Fusco, Luciano Sebastian. Universidad Nacional del Nordeste. Facultad de Cs.exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación En Proteinas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Rodríguez, Juan Pablo. Universidad Nacional del Nordeste. Facultad de Cs.exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación En Proteinas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Torres Huaco, Frank. Universidade Estadual Do Campinas. Instituto de Biología; BrasilFil: Huancahuire Vega, Salomón. Universidade Estadual Do Campinas. Instituto de Biología; BrasilFil: Teibler, Gladys Pamela. Universidad Nacional del Nordeste. Facultad de Cs.veterinarias. Departamento de Clinica. Cátedra de Farmacología; ArgentinaFil: Acosta, Ofelia Cristina. Universidad Nacional del Nordeste. Facultad de Cs.veterinarias. Departamento de Clinica. Cátedra de Farmacología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Marangoni, Sergio. Universidade Estadual Do Campinas. Instituto de Biología; BrasilFil: Ponce Soto, Luis. Universidade Estadual Do Campinas. Instituto de Biología; BrasilFil: Leiva, Laura Cristina Ana. Universidad Nacional del Nordeste. Facultad de Cs.exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación En Proteinas; ArgentinaElsevier Ireland2015-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/37476Fusco, Luciano Sebastian; Rodríguez, Juan Pablo; Torres Huaco, Frank; Huancahuire Vega, Salomón; Teibler, Gladys Pamela; et al.; P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG; Elsevier Ireland; Toxicology Letters; 238; 1; 10-2015; 7-160378-42741879-3169CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0378427415300023info:eu-repo/semantics/altIdentifier/doi/10.1016/j.toxlet.2015.06.528info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:05:36Zoai:ri.conicet.gov.ar:11336/37476instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:05:36.559CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG
title P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG
spellingShingle P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG
Fusco, Luciano Sebastian
Antivenom
Hplc-Pr
Myotoxin
Neurotoxicity
Rattlesnake
Snake Venom
title_short P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG
title_full P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG
title_fullStr P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG
title_full_unstemmed P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG
title_sort P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG
dc.creator.none.fl_str_mv Fusco, Luciano Sebastian
Rodríguez, Juan Pablo
Torres Huaco, Frank
Huancahuire Vega, Salomón
Teibler, Gladys Pamela
Acosta, Ofelia Cristina
Marangoni, Sergio
Ponce Soto, Luis
Leiva, Laura Cristina Ana
author Fusco, Luciano Sebastian
author_facet Fusco, Luciano Sebastian
Rodríguez, Juan Pablo
Torres Huaco, Frank
Huancahuire Vega, Salomón
Teibler, Gladys Pamela
Acosta, Ofelia Cristina
Marangoni, Sergio
Ponce Soto, Luis
Leiva, Laura Cristina Ana
author_role author
author2 Rodríguez, Juan Pablo
Torres Huaco, Frank
Huancahuire Vega, Salomón
Teibler, Gladys Pamela
Acosta, Ofelia Cristina
Marangoni, Sergio
Ponce Soto, Luis
Leiva, Laura Cristina Ana
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Antivenom
Hplc-Pr
Myotoxin
Neurotoxicity
Rattlesnake
Snake Venom
topic Antivenom
Hplc-Pr
Myotoxin
Neurotoxicity
Rattlesnake
Snake Venom
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Four proteins with phospholipase A2 (PLA2) activity, designated P9a(Cdt-PLA2), P9b(Cdt-PLA2), P10a(Cdt-PLA2) and P10b(Cdt-PLA2) were purified from the venom of Crotalus durissus terrificus by two chromatographic steps: a gel filtration and reversed phase HPLC. The profile obtained clearly shows that three of them have a similar abundance. The molecular mass, 14193.8340Da for P9a(Cdt-PLA2), 14134.9102Da for P9b(Cdt-PLA2), 14242.6289Da for P10a(Cdt-PLA2) and 14183.8730Da for P10b(Cdt-PLA2), were initially evaluated by SDS-PAGE and confirmed by ESI-Q-TOF spectrometry, and all of them displayed a monomeric conformation. Also, partial amino acid sequence of each protein was obtained and their alignments with other crotalic PLA2 revealed a high degree of identity among them. Additionally, we studied some pharmacological activities like neurotoxicity, myotoxicity and lethality, which prompted us to pick two of them, P9a(Cdt-PLA2) and P10a(Cdt-PLA2) that resulted to be less toxic that the others, and further characterize them to be used as immunogen. We next injected these last proteins in mice to produce antitoxins against them and ELISA and dot blots reveled that both toxins do not show immunogenic differences, unlike those other pharmacologic activities tested. Furthermore, the antibodies produced cross-reacted with all the isoforms purified demonstrating the feasibility of using only one of them and ensuring the cross-reaction of all.The results obtained show that P9a(Cdt-PLA2) isoform has the lowest toxicity and also a good purification performance; thus this protein may be a promising candidate to be employed in the production of crotalic antitoxins.
Fil: Fusco, Luciano Sebastian. Universidad Nacional del Nordeste. Facultad de Cs.exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación En Proteinas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Rodríguez, Juan Pablo. Universidad Nacional del Nordeste. Facultad de Cs.exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación En Proteinas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Torres Huaco, Frank. Universidade Estadual Do Campinas. Instituto de Biología; Brasil
Fil: Huancahuire Vega, Salomón. Universidade Estadual Do Campinas. Instituto de Biología; Brasil
Fil: Teibler, Gladys Pamela. Universidad Nacional del Nordeste. Facultad de Cs.veterinarias. Departamento de Clinica. Cátedra de Farmacología; Argentina
Fil: Acosta, Ofelia Cristina. Universidad Nacional del Nordeste. Facultad de Cs.veterinarias. Departamento de Clinica. Cátedra de Farmacología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marangoni, Sergio. Universidade Estadual Do Campinas. Instituto de Biología; Brasil
Fil: Ponce Soto, Luis. Universidade Estadual Do Campinas. Instituto de Biología; Brasil
Fil: Leiva, Laura Cristina Ana. Universidad Nacional del Nordeste. Facultad de Cs.exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación En Proteinas; Argentina
description Four proteins with phospholipase A2 (PLA2) activity, designated P9a(Cdt-PLA2), P9b(Cdt-PLA2), P10a(Cdt-PLA2) and P10b(Cdt-PLA2) were purified from the venom of Crotalus durissus terrificus by two chromatographic steps: a gel filtration and reversed phase HPLC. The profile obtained clearly shows that three of them have a similar abundance. The molecular mass, 14193.8340Da for P9a(Cdt-PLA2), 14134.9102Da for P9b(Cdt-PLA2), 14242.6289Da for P10a(Cdt-PLA2) and 14183.8730Da for P10b(Cdt-PLA2), were initially evaluated by SDS-PAGE and confirmed by ESI-Q-TOF spectrometry, and all of them displayed a monomeric conformation. Also, partial amino acid sequence of each protein was obtained and their alignments with other crotalic PLA2 revealed a high degree of identity among them. Additionally, we studied some pharmacological activities like neurotoxicity, myotoxicity and lethality, which prompted us to pick two of them, P9a(Cdt-PLA2) and P10a(Cdt-PLA2) that resulted to be less toxic that the others, and further characterize them to be used as immunogen. We next injected these last proteins in mice to produce antitoxins against them and ELISA and dot blots reveled that both toxins do not show immunogenic differences, unlike those other pharmacologic activities tested. Furthermore, the antibodies produced cross-reacted with all the isoforms purified demonstrating the feasibility of using only one of them and ensuring the cross-reaction of all.The results obtained show that P9a(Cdt-PLA2) isoform has the lowest toxicity and also a good purification performance; thus this protein may be a promising candidate to be employed in the production of crotalic antitoxins.
publishDate 2015
dc.date.none.fl_str_mv 2015-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/37476
Fusco, Luciano Sebastian; Rodríguez, Juan Pablo; Torres Huaco, Frank; Huancahuire Vega, Salomón; Teibler, Gladys Pamela; et al.; P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG; Elsevier Ireland; Toxicology Letters; 238; 1; 10-2015; 7-16
0378-4274
1879-3169
CONICET Digital
CONICET
url http://hdl.handle.net/11336/37476
identifier_str_mv Fusco, Luciano Sebastian; Rodríguez, Juan Pablo; Torres Huaco, Frank; Huancahuire Vega, Salomón; Teibler, Gladys Pamela; et al.; P9a(Cdt-PLA2) from Crotalus durissus terrificus as good immunogen to be employed in the production of crotalic anti-PLA2 IgG; Elsevier Ireland; Toxicology Letters; 238; 1; 10-2015; 7-16
0378-4274
1879-3169
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0378427415300023
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.toxlet.2015.06.528
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Ireland
publisher.none.fl_str_mv Elsevier Ireland
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.993085

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